Phase behavior and the partitioning of caveolin-1 scaffolding domain peptides in model lipid bilayers
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Horton-2006-Phase behavior and the partitioning.pdf
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Author(s)
Rädler, Joachim
Horton, Margaret R.
Gast, Alice Petry
Date Issued
October 2006
Journal
Journal of Colloid and Interface Science
Publisher
Elsevier
Citation
Horton, M, J Radler, and A Gast. “Phase Behavior and the Partitioning of Caveolin-1 Scaffolding Domain Peptides in Model Lipid Bilayers.” Journal of Colloid and Interface Science 304.1 (2006): 67–76. Web. 12 Apr. 2012. © 2006 Elsevier Inc.
Version
Final published version
Abstract
The membrane binding and model lipid raft interaction of synthetic peptides derived from the caveolin scaffolding domain (CSD) of the protein caveolin-1 have been investigated. CSD peptides bind preferentially to liquid-disordered domains in model lipid bilayers composed of cholesterol and an equimolar ratio of dioleoylphosphatidylcholine (DOPC) and brain sphingomyelin. Three caveolin-1 peptides were studied: the scaffolding domain (residues 83–101), a water-insoluble construct containing residues 89–101, and a water-soluble construct containing residues 89–101. Confocal and fluorescence microscopy investigation shows that the caveolin-1 peptides bind to the more fluid cholesterol-poor phase. The binding of the water-soluble peptide to lipid bilayers was measured using fluorescence correlation spectroscopy (FCS). We measured molar partition coefficients of 104 M−1 between the soluble peptide and phase-separated lipid bilayers and 103 M−1 between the soluble peptide and bilayers with a single liquid phase. Partial phase diagrams for our phase-separating lipid mixture with added caveolin-1 peptides were measured using fluorescence microscopy. The water-soluble peptide did not change the phase morphology or the miscibility transition in giant unilamellar vesicles (GUVs); however, the water-insoluble and full-length CSD peptides lowered the liquid–liquid melting temperature.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1016/j.jcis.2006.08.057
